• Proc. Natl. Acad. Sci. U.S.A. · Oct 1988

    Phosphorylation of serum response factor, a factor that binds to the serum response element of the c-FOS enhancer.

    • R Prywes, A Dutta, J A Cromlish, and R G Roeder.
    • Laboratory of Biochemistry and Molecular Biology, Rockefeller University, New York, NY 10021.
    • Proc. Natl. Acad. Sci. U.S.A. 1988 Oct 1;85(19):7206-10.

    AbstractSerum and growth factor regulation of c-FOS protooncogene transcription is mediated by the serum response element. A factor, serum response factor, binding to this element has already been identified. We demonstrate that serum response factor is phosphorylated in vivo on serine residues and that phosphatase treatment of this factor in vitro abolishes its DNA-binding activity. These results show phosphorylation of serum response factor to be required for its DNA-binding activity. The importance of serum response factor phosphorylation for the regulation of c-FOS expression is discussed.

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